scholarly journals Subcellular analysis of starch metabolism in developing barley seeds using a non-aqueous fractionation method

2011 ◽  
Vol 63 (5) ◽  
pp. 2071-2087 ◽  
Author(s):  
Axel Tiessen ◽  
Annika Nerlich ◽  
Benjamin Faix ◽  
Christine Hümmer ◽  
Simon Fox ◽  
...  
Keyword(s):  
Starch Metabolism ◽  
Fractionation Method

Functional Relationship of Polymerization Sites of Vertebrate Fibrinogens

1979 ◽  
Author(s):  
C Cierniewski ◽  
T Krajewski ◽  
E Janiak
Keyword(s):  
Gel Electrophoresis ◽  
Functional Relationship ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Functional Similarity ◽  
Fractionation Method ◽  
Relationship Of ◽  
Fibrin Monomers ◽  
Fibrinogen Molecule ◽  
Cold Ethanol Fractionation

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerization sites in the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces. Amphibia. Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces. Amphibia. Aves and Mammalia interacted in a specific way with immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.

Interaction of hydrolytic and phosphorolytic enzymes of starch metabolism in Kalancho� daigremontiana

Planta ◽  
1979 ◽  
Vol 147 (3) ◽  
pp. 210-215 ◽  
Author(s):  
N. Schilling ◽  
P. Dittrich
Keyword(s):  
Starch Metabolism

A rapid fractionation method for assessing key soil phosphorus parameters in agroecosystems

Geoderma ◽  
2021 ◽  
Vol 385 ◽  
pp. 114893
Author(s):  
Luciano C. Gatiboni ◽  
Leo M. Condron
Keyword(s):  
Soil Phosphorus ◽  
Fractionation Method

scholarly journals Impaired SWEET-mediated sugar transportation impacts starch metabolism in developing rice seeds

2021 ◽  
Author(s):  
Pei Li ◽  
Lihan Wang ◽  
Hongbo Liu ◽  
Meng Yuan
Keyword(s):  
Starch Metabolism ◽  
Rice Seeds

scholarly journals Acyl-CoA synthetase and the peroxisomal enzymes of β-oxidation in human liver. Quantitative analysis of their subcellular localization

1984 ◽  
Vol 224 (3) ◽  
pp. 709-720 ◽  
Author(s):  
M Bronfman ◽  
N C Inestrosa ◽  
F O Nervi ◽  
F Leighton
Keyword(s):  
Human Liver ◽  
Fatty Acyl ◽  
Single Step ◽  
Synthetase Activity ◽  
Beta Oxidation ◽  
Analysis Of Results ◽  
Fractionation Method ◽  
Hydroxyacyl Coa Dehydrogenase ◽  
Acyl Coa Oxidase ◽  
Rate Limiting

The presence of acyl-CoA synthetase (EC 6.2.1.3) in peroxisomes and the subcellular distribution of beta-oxidation enzymes in human liver were investigated by using a single-step fractionation method of whole liver homogenates in metrizamide continuous density gradients and a novel procedure of computer analysis of results. Peroxisomes were found to contain 16% of the liver palmitoyl-CoA synthetase activity, and 21% and 60% of the enzyme activity was localized in mitochondria and microsomal fractions respectively. Fatty acyl-CoA oxidase was localized exclusively in peroxisomes, confirming previous results. Human liver peroxisomes were found to contribute 13%, 17% and 11% of the liver activities of crotonase, beta-hydroxyacyl-CoA dehydrogenase and thiolase respectively. The absolute activities found in peroxisomes for the enzymes investigated suggest that in human liver fatty acyl-CoA oxidase is the rate-limiting enzyme of the peroxisomal beta-oxidation pathway, when palmitic acid is the substrate.

Starch metabolism in the fructan-grasses: Patterns of starch accumulation in excised leaves of Lolium temulentum L.

2002 ◽  
Vol 159 (3) ◽  
pp. 293-305 ◽  
Author(s):  
Andrew J. Cairns ◽  
Alan Cookson ◽  
Barry J. Thomas ◽  
Lesley B. Turner
Keyword(s):  
Starch Accumulation ◽  
Starch Metabolism ◽  
Lolium Temulentum

scholarly journals Transitory and storage starch metabolism: two sides of the same coin?

2015 ◽  
Vol 32 ◽  
pp. 143-148 ◽  
Author(s):  
James Richard Lloyd ◽  
Jens Kossmann
Keyword(s):  
Starch Metabolism ◽  
And Storage ◽  
Two Sides ◽  
Storage Starch
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